An N-Acetyltransferase-MAPK fusion protein modulates developmental reprogramming in Physcomitrium patens

ABSTRACT: Post-translational modifications (PTMs) finetune plant responses to developmental and environmental cues by impacting protein activity, stability, localization and interaction landscape. In this study we identified a moss specific protein which combines two common PTMs: acetylation and phosphorylation. This protein originated from the fusion of a MAPK with an N-acetyltransferase, for which we named it Rosetta NATD-MAPK 1 (RAK1). Using biochemical methods, we demonstrated that RAK1 has acetyltransferase activity that is enhanced by activation of its MAPK domain. Phenotypical studies of rak1 knockout mutants revealed a role for RAK1 in the regulation of the 2D-to-3D growth transition. Through mass spectrometry, we identified differential acetylation and phosphorylation events associated with metabolic reprogramming and gametophore formation in the mutants. Additional experiments also revealed that RAK1 interacts with proteins associated to several biological processes, including metabolism. Collectively, this study uncovers a previously unknown multidomain protein and provides mechanistic insights into the interplay of PTMs during developmental reprogramming.

INSTRUMENT(S):

ORGANISM(S): Physcomitrella Patens Subsp. Patens (moss)

TISSUE(S): Plant

SUBMITTER: Richard Imre  

LAB HEAD: Morten Petersen

PROVIDER: PXD071605 | Pride | 2026-04-22

REPOSITORIES: Pride